Characterization of a discontinuous epitope of the HIV envelope protein gp120 recognized by the monoclonal antibody 559/64-D by chemical modification and mass spectrometric analysis

Christine Hager-Braun; Elisabeth O. Hochleitner; Rachelle Bienstock; Miroslaw K. Gorny; Susan Zolla-Pazner; Kenneth B. Tomer

Characterization of a discontinuous epitope of the HIV envelope protein gp120 recognized by the monoclonal antibody 559/64-D by chemical modification and mass spectrometric analysis

Christine Hager-Braun, Elisabeth O. Hochleitner, Rachelle Bienstock, Miroslaw K. Gorny, Susan Zolla-Pazner, Kenneth B. Tomer

Research output: Contribution to conference › Paper › peer-review

Abstract

A discontinuous epitope of the HIV envelope protein gp120 recognized by the monoclonal antibody (mAb) 559/64-D was characterized to identify the epitopes and produce a peptide-based vaccine against HIV. The samples were analyzed by matrix-assisted laser desorption/ionization mass spectrometry (MALDI/MS). Lysine residues were partially acetylated when gp120 was bound to 559/64-D and fully acetylated with hexadeuteroacetic anhydride after separation from the mAb to characterize the epitope. The results indicate that the mAb 559/64-D recognizes an epitope which is located in close proximity and extensive structural re-arrangements occurs, affecting the regions that do not resemble the epitope.

Original language	English
Pages	427-428
Number of pages	2
State	Published - 2002
Externally published	Yes
Event	Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States Duration: 2 Jun 2002 → 6 Jun 2002

Conference

Conference	Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics
Country/Territory	United States
City	Orlando, FL
Period	2/06/02 → 6/06/02

Cite this

Hager-Braun, C., Hochleitner, E. O., Bienstock, R., Gorny, M. K., Zolla-Pazner, S., & Tomer, K. B. (2002). Characterization of a discontinuous epitope of the HIV envelope protein gp120 recognized by the monoclonal antibody 559/64-D by chemical modification and mass spectrometric analysis. 427-428. Paper presented at Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics, Orlando, FL, United States.

Hager-Braun, Christine ; Hochleitner, Elisabeth O. ; Bienstock, Rachelle et al. / Characterization of a discontinuous epitope of the HIV envelope protein gp120 recognized by the monoclonal antibody 559/64-D by chemical modification and mass spectrometric analysis. Paper presented at Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics, Orlando, FL, United States.2 p.

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title = "Characterization of a discontinuous epitope of the HIV envelope protein gp120 recognized by the monoclonal antibody 559/64-D by chemical modification and mass spectrometric analysis",

abstract = "A discontinuous epitope of the HIV envelope protein gp120 recognized by the monoclonal antibody (mAb) 559/64-D was characterized to identify the epitopes and produce a peptide-based vaccine against HIV. The samples were analyzed by matrix-assisted laser desorption/ionization mass spectrometry (MALDI/MS). Lysine residues were partially acetylated when gp120 was bound to 559/64-D and fully acetylated with hexadeuteroacetic anhydride after separation from the mAb to characterize the epitope. The results indicate that the mAb 559/64-D recognizes an epitope which is located in close proximity and extensive structural re-arrangements occurs, affecting the regions that do not resemble the epitope.",

author = "Christine Hager-Braun and Hochleitner, {Elisabeth O.} and Rachelle Bienstock and Gorny, {Miroslaw K.} and Susan Zolla-Pazner and Tomer, {Kenneth B.}",

year = "2002",

language = "English",

pages = "427--428",

note = "Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics ; Conference date: 02-06-2002 Through 06-06-2002",

}

Hager-Braun, C, Hochleitner, EO, Bienstock, R, Gorny, MK, Zolla-Pazner, S & Tomer, KB 2002, 'Characterization of a discontinuous epitope of the HIV envelope protein gp120 recognized by the monoclonal antibody 559/64-D by chemical modification and mass spectrometric analysis', Paper presented at Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics, Orlando, FL, United States, 2/06/02 - 6/06/02 pp. 427-428.

Characterization of a discontinuous epitope of the HIV envelope protein gp120 recognized by the monoclonal antibody 559/64-D by chemical modification and mass spectrometric analysis. / Hager-Braun, Christine; Hochleitner, Elisabeth O.; Bienstock, Rachelle et al.
2002. 427-428 Paper presented at Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics, Orlando, FL, United States.

Research output: Contribution to conference › Paper › peer-review

TY - CONF

T1 - Characterization of a discontinuous epitope of the HIV envelope protein gp120 recognized by the monoclonal antibody 559/64-D by chemical modification and mass spectrometric analysis

AU - Hager-Braun, Christine

AU - Hochleitner, Elisabeth O.

AU - Bienstock, Rachelle

AU - Gorny, Miroslaw K.

AU - Zolla-Pazner, Susan

AU - Tomer, Kenneth B.

PY - 2002

Y1 - 2002

N2 - A discontinuous epitope of the HIV envelope protein gp120 recognized by the monoclonal antibody (mAb) 559/64-D was characterized to identify the epitopes and produce a peptide-based vaccine against HIV. The samples were analyzed by matrix-assisted laser desorption/ionization mass spectrometry (MALDI/MS). Lysine residues were partially acetylated when gp120 was bound to 559/64-D and fully acetylated with hexadeuteroacetic anhydride after separation from the mAb to characterize the epitope. The results indicate that the mAb 559/64-D recognizes an epitope which is located in close proximity and extensive structural re-arrangements occurs, affecting the regions that do not resemble the epitope.

AB - A discontinuous epitope of the HIV envelope protein gp120 recognized by the monoclonal antibody (mAb) 559/64-D was characterized to identify the epitopes and produce a peptide-based vaccine against HIV. The samples were analyzed by matrix-assisted laser desorption/ionization mass spectrometry (MALDI/MS). Lysine residues were partially acetylated when gp120 was bound to 559/64-D and fully acetylated with hexadeuteroacetic anhydride after separation from the mAb to characterize the epitope. The results indicate that the mAb 559/64-D recognizes an epitope which is located in close proximity and extensive structural re-arrangements occurs, affecting the regions that do not resemble the epitope.

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T2 - Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics

Y2 - 2 June 2002 through 6 June 2002

ER -

Hager-Braun C, Hochleitner EO, Bienstock R, Gorny MK, Zolla-Pazner S, Tomer KB. Characterization of a discontinuous epitope of the HIV envelope protein gp120 recognized by the monoclonal antibody 559/64-D by chemical modification and mass spectrometric analysis. 2002. Paper presented at Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics, Orlando, FL, United States.

Characterization of a discontinuous epitope of the HIV envelope protein gp120 recognized by the monoclonal antibody 559/64-D by chemical modification and mass spectrometric analysis

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